An activity transition from NADH dehydrogenase to NADH oxidase during protein denaturation

Biotechnol Appl Biochem. 2018 May;65(3):286-293. doi: 10.1002/bab.1607. Epub 2017 Oct 2.

Abstract

A decrease in the specific activity of an enzyme is commonly observed when the enzyme is inappropriately handled or is stored over an extended period. Here, we reported a functional transition of an FMN-bound diaphorase (FMN-DI) that happened during the long-term storage process. It was found that FMN-DI did not simply lose its β-nicotinamide adenine diphosphate (NADH) dehydrogenase activity after a long-time storage, but obtained a new enzyme activity of NADH oxidase. Further mechanistic studies suggested that the alteration of the binding strength of an FMN cofactor with a DI protein could be responsible for this functional switch of the enzyme.

Keywords: FMN diaphorase; NADH dehydrogenase; NADH oxidase; flavoproteins; protein denaturation.

MeSH terms

  • Flavin Mononucleotide / chemistry
  • Models, Molecular
  • Molecular Structure
  • Multienzyme Complexes / metabolism*
  • NADH Dehydrogenase / metabolism*
  • NADH, NADPH Oxidoreductases / metabolism*
  • Protein Denaturation*
  • Urea / chemistry

Substances

  • Multienzyme Complexes
  • Flavin Mononucleotide
  • Urea
  • NADH oxidase
  • NADH, NADPH Oxidoreductases
  • NADH Dehydrogenase